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Abdolbaset Dabirestan, Mehran Loghmani, Gilan attaran,
Volume 13, Issue 2 (6-2024)
Abstract

This research was conducted with the aim of determining the biodiversity of Pertaran communities in three areas with mangrove cover and in 9 stations including one station in Gowatr Bay and 4 stations in each of Gowatr bay and Bahu Kalat on the eastern coast of Chabahar port. From each station, from the winter of 2019 to the fall of 2014, three sediment samples were collected seasonally for the separation and identification of sediments and one sample for the analysis of grain size and total organic matter of the sediments by Grab van Veen with a cross-sectional area of 0.028 square meters. In total, 12 genera belonging to 10 families were identified. Among the groups of the detected families of spionidae, the highest percentage of the average frequency with 13.70% was related to the Spionidae family. The survey of the density of the birds in total is 17800 ± 180 in the mentioned seasons, the average density of the birds in winter is 8720 ± 42 and the average density of the birds in the autumn is 9080 ± 181.63 in the mentioned seasons, the lowest average in winter is related to the Nereidae family: 0.5 600±67 and the most number was for Spionidae family: 1280±31.47 individuals in one square meter. The lowest average in autumn was related to the Nereidae family: 560 ± 32.65 and the highest to the Spionidae family: 1160 ± 62.94 individuals per square meter.


Volume 13, Issue 52 (4-2016)
Abstract

The natural and bioactive compounds from marine animals can be used as functional compositions for healthcare. Collagen and gelatin of marine animals could be having pharmacological and cosmetic applications. In the present study collagen was extracted from the body wall of sea cucumber (S.horrens) collected from Chahbahar Bay and its Amino acid composition was investigated. Also, gelatin from this collagen was extracted according to acidic hydrolyzed method and the functional properties were studied. The type of purified collagen was identified by the SDS-PAGE method. The results indicated the extracted collagen was the type I, because it had a α1 chain by the molecular weight of 125 KDa and a heavy band of β chain with the molecular weight of 250 KDa. The collagen contained high amount of Imino Acids and the glycine was the dominant Amino acid. The melting and gelling point of the Gelatin was 300C and 50C, respectively. The viscosity of the gelatin was 2.065 cp, lower than other fish species and mammals.                           

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